3JAZ

Atomic model of cytoplasmic polyhedrosis virus with ATP

Summary for 3JAZ

• Entry DOI: 10.2210/pdb3jaz/pdb
• Related: 3JAY 3JB0 3JB1 3JB2 3JB3
• EMDB information: 6371 6374 6375 6376 6377 6378
• Descriptor: Structural protein VP3, Capsid protein VP1, Viral structural protein 5 (3 entities in total)
• Functional Keywords: viral atpase, histidine-mediated guanylyl transfer, conformational changes, regulation of transcription, virus
• Biological source: Bombyx mori cypovirus 1 (BmCPV); More
• Total number of polymer chains: 5
• Total formula weight: 517079.87

Authors

Yu, X.K.,Jiang, J.S.,Sun, J.C.,Zhou, Z.H. (deposition date: 2015-07-06, release date: 2015-08-12, Last modification date: 2024-02-21)

Primary citation

Yu, X.,Jiang, J.,Sun, J.,Zhou, Z.H.
A putative ATPase mediates RNA transcription and capping in a dsRNA virus.
Elife, 4:e07901-e07901, 2015

PubMed Abstract: mRNA transcription in dsRNA viruses is a highly regulated process but the mechanism of this regulation is not known. Here, by nucleoside triphosphatase (NTPase) assay and comparisons of six high-resolution (2.9-3.1 Å) cryo-electron microscopy structures of cytoplasmic polyhedrosis virus with bound ligands, we show that the large sub-domain of the guanylyltransferase (GTase) domain of the turret protein (TP) also has an ATP-binding site and is likely an ATPase. S-adenosyl-L-methionine (SAM) acts as a signal and binds the methylase-2 domain of TP to induce conformational change of the viral capsid, which in turn activates the putative ATPase. ATP binding/hydrolysis leads to an enlarged capsid for efficient mRNA synthesis, an open GTase domain for His217-mediated guanylyl transfer, and an open methylase-1 domain for SAM binding and methyl transfer. Taken together, our data support a role of the putative ATPase in mediating the activation of mRNA transcription and capping within the confines of the virus.

PubMed: 26240998
DOI: 10.7554/eLife.07901

Experimental method

ELECTRON MICROSCOPY (3.1 Å)